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Here, we have shown that our approach can distinguish variation in the response to two distinct MAMP classes in Arabidopsis thaliana and identify potentially functionally significant loci. We have also demonstrated that our MAMP libraries can be used to identify candidate loci that underlie the response to MAMPs, and that strong candidates can be further validated. The utility of our approach in the MAMP field is highlighted by the fact that it can be applied to any MAMP, and hence the approach is widely applicable.
To classify the ecological role of flagellin and EF-Tu as MAMPs, it is important to determine whether the responses evoked by the two elicitors are functionally distinct. The ecological role of the two elicitors was assessed in terms of their correlations within each class. This analysis was carried out using our 186 genotypes of A. thaliana panel that were originally used by Atwell et al. [ 21 ]. All of the plants from that panel had been phenotyped for SGI using flg22 and elf18 MAMPs.
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Do the differences found for flg22- and elf18-induced SGI reflect phenotypic variations previously described for these two MAMPs? To answer this question, we first assessed the known sequence variation of the two major flg22 isoforms (flg22Pv and flg22DC) that were studied here [ 23 ]. The amino acid sequences of the 15 different variants were aligned in supplementary file myflg22_alleles.txt. The length of the aligned regions ranged from 97 to 102 amino acids for elf18. As structural changes in the N-terminal region of the peptide might affect the ligand binding sites of the receptor we also aligned the N-terminal sequences of flg22 (98 amino acids) and elf18 (99 amino acids) which are completely encoded by the gene FLS2 [ 8 ]. A comparison of their length revealed more variability in the flg22 peptide than elf18. Three amino acid insertions (sup Leu in position 8, Leu – Tyr – Leu – Tyr – Thr – Leu – Lys – Arg in position 14, Leu – Tyr – Ala – Leu in position 26 and Leu – Tyr in position 31 ) were observed for flg22DC, whereas only a Ser – Thr amino acid insertion in position 29 was observed for flg22Pv.
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Sequences of P. syringae strains were obtained from the NCBI database. Plant proteins were identified by BlastP searches of the NCBI nr protein database using the protein sequences of P. syringae strains, downloaded from the NCBI database, and the plant protein sequences of the TAIR10 database. Plasmids used to create MAMP variants were purified using Qiagen kits. Production of MAMP variants and their quantification was performed as described before [ 3 ]. Protein concentrations were determined using the Bradford protein assay [ 44 ].
The concentration of synthetic MAMPs were verified by mass spectrometry and their purity was additionally confirmed by SDS-PAGE and silver-stained gels. For HR assays the P. syringae strains were grown at room temperature on King’s B agar medium (potato dextrose agar, no starch) plates for 48 hours. Cell cultures were prepared by suspending P. syringae cells in liquid King’s B medium for 1 hour, followed by centrifugation for 5 minutes at 4°C and 10 minutes at room temperature and by resuspending the bacterial pellet in sterile water to an optical density at 600 nm of 1.0. This culture suspension was spread onto the surface of King’s B agar plates. The plates were placed in Petri dishes and incubated at room temperature for 48 hours. Five microliters of each MAMP variant was used to inoculate the bacterial cell cultures. Flg22 was included as a positive control. The plates were incubated at room temperature for 48 hours and inspected for cell death. Results were quantified by measuring the diameter of the clearing zone surrounding bacterial colonies and cell death was calculated as the percentage of the total (“−” indicates no cell death or clearing zone).
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MAMP PRO 18.104.22.16898 System Requirements
- Windows XP or later
- 32-bit or 64-bit edition
- Mac OS 10.6 or later
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